Effects of Hypoxia and Radiation-Induced Exosomes on Migration of Lung Cancer Cells and Angiogenesis of Umbilical Vein Endothelial Cells

2020 ◽  
Vol 194 (1) ◽  
pp. 71
Author(s):  
Fang Mo ◽  
Yanwu Xu ◽  
Junling Zhang ◽  
Lin Zhu ◽  
Chen Wang ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Endothelial Cells ◽  
Cancer Cells ◽  
Umbilical Vein ◽  
Lung Cancer Cells ◽  
Radiation Induced ◽  
Umbilical Vein Endothelial Cells

scholarly journals Protein C inhibits endocytosis of thrombin-thrombomodulin complexes in A549 lung cancer cells and human umbilical vein endothelial cells

Blood ◽  
1987 ◽  
Vol 69 (5) ◽  
pp. 1481-1484 ◽  
Author(s):  
I Maruyama ◽  
PW Majerus
Keyword(s):  
Lung Cancer ◽  
Endothelial Cells ◽  
Cancer Cells ◽  
Protein C ◽  
Umbilical Vein ◽  
Protein S ◽  
Lung Cancer Cells ◽  
Human Lung Cancer ◽  
Umbilical Vein Endothelial Cells

Abstract We investigated the effect of protein C on the endocytosis of thrombin- thrombomodulin complexes. We previously showed that exposure of umbilical vein endothelial cells to thrombin stimulated the internalization and degradation of thrombin. A similar internalization was stimulated by a monoclonal antithrombomodulin antibody. We have repeated these studies in the presence of protein C and found that endocytosis of 125I-thrombin-thrombomodulin complexes, but not 125I- antithrombomodulin-thrombomodulin complexes, is inhibited. Activated protein C did not inhibit endocytosis of thrombin-thrombomodulin complexes. Protein C inhibited both internalization and degradation of 125I-thrombin and diisopropylphosphoryl (DIP) 125I-thrombin in human lung cancer cells (A549). These effects were observed at protein C concentrations found in human plasma. Protein S had no effect on the inhibition of endocytosis of thrombin-thrombomodulin complexes by protein C. We propose that protein C may regulate the rate of endocytosis of thrombin-thrombomodulin complexes in vivo and thereby control the capacity for endothelium to activate protein C.

scholarly journals Protein C inhibits endocytosis of thrombin-thrombomodulin complexes in A549 lung cancer cells and human umbilical vein endothelial cells

Blood ◽  
1987 ◽  
Vol 69 (5) ◽  
pp. 1481-1484 ◽  
Author(s):  
I Maruyama ◽  
PW Majerus
Keyword(s):  
Lung Cancer ◽  
Endothelial Cells ◽  
Cancer Cells ◽  
Protein C ◽  
Umbilical Vein ◽  
Protein S ◽  
Lung Cancer Cells ◽  
Human Lung Cancer ◽  
Umbilical Vein Endothelial Cells

We investigated the effect of protein C on the endocytosis of thrombin- thrombomodulin complexes. We previously showed that exposure of umbilical vein endothelial cells to thrombin stimulated the internalization and degradation of thrombin. A similar internalization was stimulated by a monoclonal antithrombomodulin antibody. We have repeated these studies in the presence of protein C and found that endocytosis of 125I-thrombin-thrombomodulin complexes, but not 125I- antithrombomodulin-thrombomodulin complexes, is inhibited. Activated protein C did not inhibit endocytosis of thrombin-thrombomodulin complexes. Protein C inhibited both internalization and degradation of 125I-thrombin and diisopropylphosphoryl (DIP) 125I-thrombin in human lung cancer cells (A549). These effects were observed at protein C concentrations found in human plasma. Protein S had no effect on the inhibition of endocytosis of thrombin-thrombomodulin complexes by protein C. We propose that protein C may regulate the rate of endocytosis of thrombin-thrombomodulin complexes in vivo and thereby control the capacity for endothelium to activate protein C.

scholarly journals Resveratrol enhances ionizing radiation-induced premature senescence in lung cancer cells

2013 ◽  
Vol 43 (6) ◽  
pp. 1999-2006 ◽  
Author(s):  
HONGMEI LUO ◽  
LU WANG ◽  
BRADLEY A. SCHULTE ◽  
AIMIN YANG ◽  
SHENGSONG TANG ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Ionizing Radiation ◽  
Cancer Cells ◽  
Lung Cancer Cells ◽  
Premature Senescence ◽  
Radiation Induced
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